title: On the stereochemistry of 2-hydroxyethylphosphonate dioxygenase.
abstract: Stereochemical investigations have shown that the conversion of 2-hydroxyethylphosphonate to hydroxymethylphosphonate by the enzyme HEPD involves removal of the pro-S hydrogen at C2 and, surprisingly, the loss of stereochemical information at C1. As a result, the mechanisms previously proposed for HEPD must be re-evaluated.
authors.affiliation: Howard Hughes Medical Institute and Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
authors.forename: John T
authors.initials: JT
authors.lastname: Whitteck
authors.forename: Petra
authors.initials: P
authors.lastname: Malova
authors.forename: Spencer C
authors.initials: SC
authors.lastname: Peck
authors.forename: Robert M
authors.initials: RM
authors.lastname: Cicchillo
authors.forename: Friedrich
authors.initials: F
authors.lastname: Hammerschmidt
authors.forename: Wilfred A
authors.initials: WA
authors.lastname: van der Donk
mesh_terms: D049308:Dioxygenases / Q000737:chemistry* / Q000378:metabolism; D015394:Molecular Structure; D063065:Organophosphonates / Q000737:chemistry*; D013237:Stereoisomerism
chemical_list: C519566:2-hydroxyethyl phosphonate; D063065:Organophosphonates; D049308:Dioxygenases